HIGH-SPEED SINGLE-MOLECULE STUDIES OF THE STRUCTURE AND FUNCTION OF NUCLEAR PORE COMPLEX PDF Download
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Author: Yichen Li
Publisher:
ISBN:
Category :
Languages : en
Pages : 112
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Book Description
Author: Joseph M. Kelich
Publisher:
ISBN:
Category :
Languages : en
Pages : 115
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Book Description
Nuclear pore complexes (NPCs) are large macromolecular gateways embedded in the nuclear envelope of Eukaryotic cells that serve to regulate bi-directional trafficking of particles to and from the nucleus. NPCs have been described as creating a selectively permeable barrier mediating the nuclear export of key endogenous cargoes such as mRNA, and pre-ribosomal subunits as well as allow for the nuclear import of nuclear proteins and some viral particles. Remarkably, other particles that are not qualified for nucleocytoplasmic transport are repelled from the NPC, unable to translocate. The NPC is made up of over 30 unique proteins, each present in multiples of eight copies. The two primary protein components of the NPC can be simplified as scaffold nucleoporins which form the main structure of the NPC and the phenylalanine-glycine (FG) motif containing nucleoporins (FG-Nups) which anchor to the scaffold and together create the permeability barrier within the pore. Advances in fluorescence microscopy techniques including single-molecule and super-resolution microscopy have made it possible to label and visualize the dynamic components of the NPC as well as track the rapid nucleocytoplasmic transport process of importing and exporting cargoes. The focus of this dissertation will be on live cell fluorescence microscopy application in probing the dynamic components of the NPC as well as tracking the processes of nucleocytoplasmic transport.
Author: Yichen Li
Publisher:
ISBN:
Category :
Languages : en
Pages : 112
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Book Description
Author:
Publisher: Elsevier
ISBN: 0124171788
Category : Science
Languages : en
Pages : 553
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Book Description
Volume 122 of Methods in Cell Biology describes modern tools and techniques used to study nuclear pore complexes and nucleocytoplasmic transport in diverse eukaryotic model systems (including mammalian cells, Xenopus, C. elegans, yeast). The volume enables investigators to analyze nuclear pore complex structure, assembly, and dynamics; to evaluate protein and RNA trafficking through the nuclear envelope; and to design in vivo or in vitro assays appropriate to their research needs. Beyond the study of nuclear pores and transport as such, these protocols will also be helpful to scientists characterizing gene regulation, signal transduction, cell cycle, viral infections, or aging. The NPC being one of the largest multiprotein complexes in the cell, some protocols will also be of interest for people currently characterizing other macromolecular assemblies. This book is thus designed for laboratory use by graduate students, technicians, and researchers in many molecular and cellular disciplines. Describes modern tools and techniques used to study nuclear pore complexes and nucleocytoplasmic transport in diverse eukaryotic model systems (mammalian cells, Xenopus, C. elegans, yeast) Chapters are written by experts in the field Cutting-edge material
Author: Reiner Peters
Publisher: Springer Science & Business Media
ISBN: 3642715656
Category : Science
Languages : en
Pages : 296
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Book Description
Author: Isabel Mary McMorrow
Publisher:
ISBN:
Category : Biological transport
Languages : en
Pages : 346
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Book Description
Author: Bruce Alberts
Publisher:
ISBN: 9780815332183
Category : Cytology
Languages : en
Pages : 0
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Book Description
Author: Jeffrey Hsin Nien Tang
Publisher:
ISBN:
Category :
Languages : en
Pages : 103
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Book Description
The nuclear pore complex (NPC) is one of the largest known protein structures in the cell. Evolutionarily conserved in eukaryotes ranging from fungi to plants and animals, the NPC is the main transporter of molecules between the cell cytoplasm and nucleus. Maintaining the proper compartment-specific localization of proteins and RNA is crucial for normal cell function, and the nuclear pore accomplishes this task both robustly and efficiently. Over the past several decades, insight into the composition, organization, structure, and mechanism of the NPC has been gradually teased out through careful experimentation. However, many questions about the pore's function remain unanswered. In this dissertation, I describe efforts aimed at elucidating several aspects of the NPC. First, I investigate the transport properties of the pore, specifically looking at how the nuclear transport receptor importin-[beta] and the Ran GTPase interact not only with each other but also how they may affect the pore itself. The nucleoporin Nup153 is identified as an important player in the nuclear transport process which binds strongly to importin-[beta] in a Ran-sensitive manner. Using multiple experimental techniques, the properties of importin-[beta], and Nup153's interactions are characterized and shown to be capable of modulating the selective permeability barrier of the NPC. Next, I examine how members of a major class of nuclear pore proteins, the scaffold nucleoporins, are both structurally and functionally similar to the karyopherin family of soluble nuclear transport receptors. Structures of the proteins Nup188 and Nup192 are analyzed and shown to resemble those of karyopherins. Furthermore, in vitro assays indicate that at least a subset of the scaffold nucleoporins behave functionally as transport receptors, hinting at an evolutionary relationship between these two important classes of proteins. Finally, a calcium-mediated phenomenon affecting the permeability of the NPC is explored. I show that certain cytosolic proteases are activated by millimolar concentrations of calcium ion which leads irreversibly to an increase in the nuclear pore's permeability to large molecules. A model for physiological pathways implicated in this effect is proposed.
Author: Krishna Chaitanya Mudumbi
Publisher:
ISBN:
Category :
Languages : en
Pages : 111
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Book Description
The nucleus of eukaryotic cells is a vitally important organelle that sequesters the genetic information of the cell, and protects it with the help of two highly evolved structures, the nuclear envelope (NE) and nuclear pore complexes (NPCs). Together, these two structures mediate the bidirectional trafficking of molecules between the nucleus and cytoplasm by forming a barrier. NE transmembrane proteins (NETs) embedded in either the outer nuclear membrane (ONM) or the inner nuclear membrane (INM) play crucial roles in both nuclear structure and functions, including: genome architecture, epigenetics, transcription, splicing, DNA replication, nuclear structure, organization and positioning. Furthermore, numerous human diseases are associated with mutations and mislocalization of NETs on the NE. There are still many fundamental questions that are unresolved with NETs, but we focused on two major questions: First, the localization and transport rate of NETs, and second, the transport route taken by NETs to reach the INM. Since NETs are involved with many of the mechanisms used to maintain cellular homeostasis, it is important to quantitatively determine the spatial locations of NETs along the NE to fully understand their role in these vital processes. However, there are limited available approaches for this task, and moreover, these methods provide no information about the translocation rates of NETs between the two membranes. Furthermore, while the trafficking of soluble proteins between the cytoplasm and the nucleus has been well studied over the years, the path taken by NETs into the nucleus remains in dispute. At least four distinct models have been proposed to suggest how transmembrane proteins destined for the INM cross the NE through NPC-dependent or NPC-independent mechanisms, based on specific features found on the soluble domains of INM proteins. In order to resolve these two major questions, it is necessary to employ techniques with the capabilities to observe these dynamics at the nanoscale. Current experimental techniques are unable to break the temporal and spatial resolution barriers required to study these phenomena. Therefore, we developed and modified single-molecule techniques to answer these questions. First, to study the distribution of NETs on the NE, we developed a new single-molecule microscopy method called single-point single-molecule fluorescence recovery after photobleaching (smFRAP), which is able to provide spatial resolution
Author: Irwin M. Arias
Publisher: John Wiley & Sons
ISBN: 1119436826
Category : Medical
Languages : en
Pages : 1156
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Book Description
Bridging the gap between basic scientific advances and the understanding of liver disease — the extensively revised new edition of the premier text in the field. The latest edition of The Liver: Biology and Pathobiology remains a definitive volume in the field of hepatology, relating advances in biomedical sciences and engineering to understanding of liver structure, function, and disease pathology and treatment. Contributions from leading researchers examine the cell biology of the liver, the pathobiology of liver disease, the liver’s growth, regeneration, metabolic functions, and more. Now in its sixth edition, this classic text has been exhaustively revised to reflect new discoveries in biology and their influence on diagnosing, managing, and preventing liver disease. Seventy new chapters — including substantial original sections on liver cancer and groundbreaking advances that will have significant impact on hepatology — provide comprehensive, fully up-to-date coverage of both the current state and future direction of hepatology. Topics include liver RNA structure and function, gene editing, single-cell and single-molecule genomic analyses, the molecular biology of hepatitis, drug interactions and engineered drug design, and liver disease mechanisms and therapies. Edited by globally-recognized experts in the field, this authoritative volume: Relates molecular physiology to understanding disease pathology and treatment Links the science and pathology of the liver to practical clinical applications Features 16 new “Horizons” chapters that explore new and emerging science and technology Includes plentiful full-color illustrations and figures The Liver: Biology and Pathobiology, Sixth Edition is an indispensable resource for practicing and trainee hepatologists, gastroenterologists, hepatobiliary and liver transplant surgeons, and researchers and scientists in areas including hepatology, cell and molecular biology, virology, and drug metabolism.
Author: Christophe Lavelle
Publisher: Academic Press
ISBN: 012803503X
Category : Science
Languages : en
Pages : 620
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Book Description
Nuclear Architecture and Dynamics provides a definitive resource for (bio)physicists and molecular and cellular biologists whose research involves an understanding of the organization of the genome and the mechanisms of its proper reading, maintenance, and replication by the cell. This book brings together the biochemical and physical characteristics of genome organization, providing a relevant framework in which to interpret the control of gene expression and cell differentiation. It includes work from a group of international experts, including biologists, physicists, mathematicians, and bioinformaticians who have come together for a comprehensive presentation of the current developments in the nuclear dynamics and architecture field. The book provides the uninitiated with an entry point to a highly dynamic, but complex issue, and the expert with an opportunity to have a fresh look at the viewpoints advocated by researchers from different disciplines. Highlights the link between the (bio)chemistry and the (bio)physics of chromatin Deciphers the complex interplay between numerous biochemical factors at task in the nucleus and the physical state of chromatin Provides a collective view of the field by a large, diverse group of authors with both physics and biology backgrounds
